2024
Dual function of LapB (YciM) in regulating Escherichia coli lipopolysaccharide synthesis
Shu S, Tsutsui Y, Nathawat R, Mi W. Dual function of LapB (YciM) in regulating Escherichia coli lipopolysaccharide synthesis. Proceedings Of The National Academy Of Sciences Of The United States Of America 2024, 121: e2321510121. PMID: 38635633, PMCID: PMC11046580, DOI: 10.1073/pnas.2321510121.Peer-Reviewed Original ResearchConceptsLPS synthesisTetratricopeptide repeatCytoplasmic domainLevels of lipopolysaccharideCryo-EM structureGram-negative bacteriaLipopolysaccharide synthesisProtease FtsHRubredoxin domainLpxC activityTransmembrane helicesIn vivo analysisLpxCPseudomonas aeruginosaEnzymatic activityLapBFtsHAllosteric effectsYciMDual functionIn vitroTetratricopeptideAdaptorMotifDeacetylase
2022
Biochemical and structural basis for differential inhibitor sensitivity of EGFR with distinct exon 19 mutations
van Alderwerelt van Rosenburgh I, Lu D, Grant M, Stayrook S, Phadke M, Walther Z, Goldberg S, Politi K, Lemmon M, Ashtekar K, Tsutsui Y. Biochemical and structural basis for differential inhibitor sensitivity of EGFR with distinct exon 19 mutations. Nature Communications 2022, 13: 6791. PMID: 36357385, PMCID: PMC9649653, DOI: 10.1038/s41467-022-34398-z.Peer-Reviewed Original Research
2021
Structural basis for ligand reception by anaplastic lymphoma kinase
Li T, Stayrook SE, Tsutsui Y, Zhang J, Wang Y, Li H, Proffitt A, Krimmer SG, Ahmed M, Belliveau O, Walker IX, Mudumbi KC, Suzuki Y, Lax I, Alvarado D, Lemmon MA, Schlessinger J, Klein DE. Structural basis for ligand reception by anaplastic lymphoma kinase. Nature 2021, 600: 148-152. PMID: 34819665, PMCID: PMC8639777, DOI: 10.1038/s41586-021-04141-7.Peer-Reviewed Original Research
2011
Chapter Fifteen Probing Serpin Conformational Change Using Mass Spectrometry and Related Methods
Tsutsui Y, Sarkar A, Wintrode P. Chapter Fifteen Probing Serpin Conformational Change Using Mass Spectrometry and Related Methods. Methods In Enzymology 2011, 501: 325-350. PMID: 22078541, PMCID: PMC3679668, DOI: 10.1016/b978-0-12-385950-1.00015-8.Peer-Reviewed Original ResearchConceptsStructural mass spectrometry techniquesHydrogen/deuterium exchangeMass spectrometry techniquesDeuterium exchangeIon mobility mass spectrometrySpectrometry techniquesMass spectrometryMobility mass spectrometrySerpin polymersConformational flexibilitySerpin functionSerpin polymerizationChemical footprintingConformational changesThermodynamic metastabilitySpectrometryChapter FifteenSerpinsStructural distributionPolymerizationPolymersStabilityMisfoldingInhibitory mechanismFootprinting
2009
Local and Global Effects of a Cavity Filling Mutation in a Metastable Serpin
Sengupta T, Tsutsui Y, Wintrode P. Local and Global Effects of a Cavity Filling Mutation in a Metastable Serpin. Biochemistry 2009, 48: 8233-8240. PMID: 19624115, PMCID: PMC2746415, DOI: 10.1021/bi900342d.Peer-Reviewed Original Research